Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HAV-228

Background:

Forty-two antigenic domains were identified across the hepatitis A virus (HAV) polyprotein by using a set of 237 overlapping 20-mer synthetic peptides spanning the entire HAV polyprotein and a panel of serum samples from acutely HAV-infected patients. The term "antigenic domain" is used in this study to define a protein region spanned with consecutive overlapping immunoreactive peptides. Nineteen antigenic domains were found within the structural proteins, and 22 were found within the nonstructural proteins, with 1 domain spanning the junction of VP1 and P2A proteins. Five of these domains were considered immunodominant, as judged by both the breadth and the strength of their immunoreactivity. One domain is located within the VP2 protein at position 57-90 aa. A second domain, located at position 767-842 aa, contains the C-terminal part of the VP1 protein and the entire P2A protein. A third domain, located at position 1403-1456 aa, comprises the C-terminal part of the P2C protein and the N-terminal half of the P3A protein. The fourth domain, located at position 1500-1519 aa, includes almost the entire P3B, and the last domain, located at position 1719-1764 aa, contains the C-terminal region of the P3C protein and the N-terminal region of the P3D protein. It is interesting to note that four of the five most immunoreactive domains are derived from small HAV proteins and/or encompass protein cleavage sites separating different HAV proteins.

Description :

The protein contains the HAV Coat protein VP1 and core protein P2A immunodominant regions, amino acids: (722-830 a.a.). HAV core proteins are purified by proprietary chromatographic techniques.

Purification method:

Purified by proprietary chromatographic technique.

Purity:

Protein is >90% pure as determined by 10% PAGE (coomassie staining).

Formulation:

5.9mg/ml. 1mg in 10mM Tris0Hcl, pH4.5, 100mM Sodium Phosphate and 8M urea.

Storage:

Recombinant HAV is shipped at ambient temperature. Upon arrival, Store at -20C.

Stability:

Recombinant HAV is stable 5 years frozen, One month in solution at room temperature.

Specificity:

Immunoreactive with sera of HAV-infected individuals

Application:

Recombinant HAV Antigen may be used in ELISA and Western blots, excellent for detection of HAV with minimal specificity problems.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Protein synonyms/aliases:

Genome polyprotein

Precursor's functional components:

Coat protein VP4 (P1A)
Coat protein VP2(P1B)
Coat protein VP3 (P1C)
Coat protein VP1 (P1D)
Picornain 2A(EC 3.4.22.29)
    (Core protein P2A)
Core protein P2B
Core protein P2C;Probable protein P3A
Probable protein P3B
Picornain 3C(EC 3.4.22.28)
    (Protease 3C)
    (P3C)
RNA-directed RNA polymerase(EC 2.7.7.48)
    (P3D) .

Protein Family:

Protein Domains:

Domains:
•IPR001676   Picornavirus capsid
•IPR000605   RNA helicase
•IPR000199   Peptidase C3A and C3B, picornaviral
•IPR007095   RNA-directed RNA polymerase, double-strand and positive-strand RNA virus
•IPR001205   RNA-directed RNA polymerase, P3D protein

Protein links:

Precursor- Protein structure and amino acid sequence:

Latest Publications:

1. Liposome entrapment and immunogenic studies of a synthetic lipophilic multiple antigenic peptide bearing VP1 and VP3 domains of the hepatitis A virus: a robust method for vaccine design.
FEBS Lett 2003 Apr 10;540(1-3):133-40
2. Molecular evolution of hepatitis A virus: a new classification based on the complete VP1 protein.
J Viro l 2002 Sep;76(18):9516-25
3. Identification of VP1/2A and 2C as virulence genes of hepatitis A virus and demonstration of genetic instability of 2C.
J Virol 2002 Sep;76(17):8551-9
4. A proposed vestigial translation initiation motif in VP1 of hepatitis A virus.
Virus Res 2002 Jul;87(1):11-9
5. Maturation of the hepatitis A virus capsid protein VP1 is not dependent on processing by the 3Cpro proteinase.
J Virol 1999 Aug;73(8):6220-7
6. Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus.
J Virol 1999 Jul;73(7):6015-23

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中華民國95年06月06日更新